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Database: UniProt
Entry: A0A059J546_TRIIM
LinkDB: A0A059J546_TRIIM
Original site: A0A059J546_TRIIM 
ID   A0A059J546_TRIIM        Unreviewed;       455 AA.
AC   A0A059J546;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Protein-tyrosine phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=H109_05467 {ECO:0000313|EMBL:KDB22597.1};
OS   Trichophyton interdigitale (strain MR816).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB22597.1, ECO:0000313|Proteomes:UP000024533};
RN   [1] {ECO:0000313|EMBL:KDB22597.1, ECO:0000313|Proteomes:UP000024533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR816 {ECO:0000313|EMBL:KDB22597.1,
RC   ECO:0000313|Proteomes:UP000024533};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA   Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA   Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA   Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Trichophyton interdigitale MR816.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDB22597.1}.
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DR   EMBL; AOKY01000345; KDB22597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059J546; -.
DR   STRING; 1215338.A0A059J546; -.
DR   HOGENOM; CLU_001645_9_12_1; -.
DR   OMA; HYLFAGW; -.
DR   Proteomes; UP000024533; Unassembled WGS sequence.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd18533; PTP_fungal; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000024533}.
FT   DOMAIN          88..351
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          260..342
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..455
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  50881 MW;  4459BFFDE65F8122 CRC64;
     MAEVNLSASL SKRSRSTDSR VSAGQCSDAS DTDGKPAHGK PAVPSYLNQP AKYVRDKFSE
     LEWMERHRRA AGALSQDPTH KWMLDTSPQV KARNRYGDVQ AWENCRVHLK VPAGECDFIN
     ASPIVLKDPE TDGEYKYIAS QGPKRDRLAD FWNMIYHEAG EVAVLVMLTQ TVESGKEKCA
     QYFPQDMENP TFEFSSHSTT EPPDAHFSGS VTLLNTTYDE SIRSHVSELE LRVGSNTKTV
     WHFLFAGWSD YGTPEGPDRD ALLNLMTATA EKAKSFSNPR IVHCSAGVGR TGTFIALDHL
     LRQLQSGQLL KADDKSADAV FNTVNRLREQ RMLMVYNAFQ YQFIYDVLKE QTQIKLGIQS
     APIEPRPQKI AKPDDGMFKP ELVALSPADI GSAAEPDDPE SENNETKDVG RDKESKGDKE
     NNDNHEADDD DDDDDDDDDE DDEDDDDEAE DEDES
//
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